Austin Christopher J D, Astelbauer Florian, Kosim-Satyaputra Priambudi, Ball Helen J, Willows Robert D, Jamie Joanne F, Hunt Nicholas H
Molecular Immunopathology Unit, Bosch Institute, University of Sydney, Sydney, Australia.
Amino Acids. 2009 Jan;36(1):99-106. doi: 10.1007/s00726-008-0037-6. Epub 2008 Feb 15.
The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the alpha-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next.
血红素蛋白吲哚胺2,3-双加氧酶（IDO）是哺乳动物色氨酸代谢最重要途径中的首个限速酶。近年来，它受到了广泛关注，特别是因其在免疫和多种疾病发病机制中的双重作用。本文报道了重组人IDO和重组小鼠IDO在生化行为和结构特征方面的异同。在底物转化和pH稳定性方面观察到了显著差异。还注意到抑制剂效力和热稳定性的差异。二级结构特征大致相似，但不同物种之间存在明显差异，特别是在酶的α-螺旋部分。在用小鼠模型替代人类疾病时，在将一个系统的实验结果应用于另一个系统之前，必须认识到小鼠和人类IDO之间的差异。
